Abstract
Alginate oligosaccharides (AOS) show versatile bioactivities. Although various alginate lyases have been characterized, enzymes with special characteristics are still rare. In this study, a polysaccharide lyase family 7 (PL7) alginate lyase-encoding gene, aly08, was cloned from the marine bacterium Vibrio sp. SY01 and expressed in Escherichia coli. The purified alginate lyase Aly08, with a molecular weight of 35 kDa, showed a specific activity of 841 U/mg at its optimal pH (pH 8.35) and temperature (45 °C). Aly08 showed good pH-stability, as it remained more than 80% of its initial activity in a wide pH range (4.0–10.0). Aly08 was also a thermo-tolerant enzyme that recovered 70.8% of its initial activity following heat shock treatment for 5 min. This study also demonstrated that Aly08 is a polyG-preferred enzyme. Furthermore, Aly08 degraded alginates into disaccharides and trisaccharides in an endo-manner. Its thermo-tolerance and pH-stable properties make Aly08 a good candidate for further applications.
Highlights
Alginate is an acidic hetero-polysaccharide extracted from brown algae, which accounting for22–44% of its dry weight [1,2,3]
Alginate lyase (E.C. 4.2.2.3 and E.C. 4.2.2.11) is a kind of polysaccharide lyase that degrades alginate by β-eliminating the glycoside 1-4 O-bonds between C4 and C5 at the non-reducing end, producing unsaturated alginate oligosaccharides (UAOS) as main products [6,7]
According to the Carbohydrate-Active enZYmes (CAZy) databases, alginate lyases belong to PL families 5, 6, 7, 14, 15, 17, and 18 based on the analysis of their amino acid sequences [10,11,12]
Summary
Alginate is an acidic hetero-polysaccharide extracted from brown algae, which accounting for. Hundreds of alginate lyases have been purified, cloned, and characterized from marine microorganisms, brown seaweeds, and mollusks [15,16,17,18] These reported enzymes with characteristics specific for commercial use are rare. There is an urgency to obtain an alginate lyase with the optimal characteristics (e.g., pH-stability, thermo-tolerance, and single product distribution) needed for industrial applications. This study revealed that Aly was a polyG-preferred enzyme with special characteristics, such as wide pH-stability, thermo-tolerance, and single product distribution. These special features suggest that Aly may play essential roles in saccharification processes of alginate and carbon cycling
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